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Isolation and Properties of Two sialate-O-acetylesterases From Horse Liver With 4- And 9-O-acetyl Specificities

Isolation and Properties of Two sialate-O-acetylesterases From Horse Liver With 4- And 9-O-acetyl Specificities

Roland Schauer, Ashok K Shukla

Glycoconj J. 2008 Oct;25(7):625-32.

PMID: 18246423

Abstract:

Sialate-O-acetylesterase was purified almost 900-fold from particle-free supernatants of horse liver by gel filtration, ion-exchange chromatography and isoelectric focussing. The native enzyme on gel filtration exhibits a molecular weight of 54,000 Da. It was separated by isoelectric focussing into two forms with pI values of 4.8 and 5.7, respectively. The esterase with a lower pI hydrolyses only 9-O-acetyl groups from sialic acids (K(M) 1.1 mM), while that with the higher pI esterifies both 4- and 9-O-acetylated monosaccharides at similar rates (K(M) 0.3 M and 1.3 mM, respectively). Both forms are inactive with 7-O-acetylated N-acetylneuraminic acid. Enzyme assays were carried out at the pH optimum (pH 8.4-8.6) using free O-acetylated sialic acids followed by direct analysis of the reaction products by isocratic anion-exchange HPLC. Glycosidically bound sialic acids can also be de-O-acetylated. Horse liver esterase seems to be an essential enzyme for the catabolism of 4-O-acetylated sialoglycoconjugates, since sialidase from this tissue cannot act on 4-O-acetylated sialic acids.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9016186-D	Esterase from horse liver		9016-18-6	Price

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